MraZ from Escherichia coli:: cloning, purification, crystallization and preliminary X-ray analysis

被引:9
|
作者
Adams, MA [1 ]
Udell, CM [1 ]
Pal, GP [1 ]
Jia, ZC [1 ]
机构
[1] Queens Univ, Dept Biochem, Kingston, ON K7L 3N6, Canada
关键词
D O I
10.1107/S1744309105007657
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The MraZ family of proteins, also referred to as the UPF0040 family, are highly conserved in bacteria and are thought to play a role in cell-wall biosynthesis and cell division. The murein region A (mra) gene cluster encodes MraZ proteins along with a number of other proteins involved in this complex process. To date, there has been no clear functional assignment provided for MraZ proteins and the structure of a homologue from Mycoplasma pneumoniae, MPN314, failed to suggest a molecular function. The b0081 gene from Escherichia coli that encodes the MraZ protein was cloned and the protein was overexpressed, purified and crystallized. This data is presented along with evidence that the E. coli homologue exists in a different oligomeric state to the MPN314 protein.
引用
收藏
页码:378 / 380
页数:3
相关论文
共 50 条
  • [1] MdaB from Escherichia coli:: cloning, purification, crystallization and preliminary X-ray analysis
    Adams, MA
    Iannuzzi, P
    Jia, Z
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2005, 61 : 235 - 238
  • [2] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli
    Li, Ming
    Qiu, Xi
    Su, Chih-Chia
    Long, Feng
    Gu, Ruoyu
    McDermott, Gerry
    Yu, Edward W.
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2006, 62 : 1150 - 1152
  • [3] Purification, crystallization and preliminary X-ray analysis of the Escherichia coli phytase
    Jia, ZC
    Golovan, S
    Ye, QL
    Forsberg, CW
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1998, 54 : 647 - 649
  • [4] Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli
    Blanco, J
    Viola, RE
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2002, 58 : 352 - 354
  • [5] Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli
    van Straaten, KE
    Dijkstra, GBW
    Thunnissen, MAWH
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 : 758 - 760
  • [6] Crystallization and preliminary X-ray analysis of FlhD from Escherichia coli
    Campos, A
    Matsumura, P
    Volz, K
    JOURNAL OF STRUCTURAL BIOLOGY, 1998, 123 (03) : 269 - 271
  • [7] Crystallization and preliminary X-ray analysis of α-xylosidase from Escherichia coli
    Kitamura, M
    Ose, T
    Okuyama, M
    Watanabe, H
    Yao, M
    Mori, H
    Kimura, A
    Tanaka, I
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2005, 61 : 178 - 179
  • [8] Crystallization and preliminary X-ray analysis of Mlc from Escherichia coli
    Gerber, K
    Boos, W
    Welte, W
    Schiefner, A
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2005, 61 : 183 - 185
  • [9] Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase
    Lemke, C
    Yeung, M
    Howell, PL
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1999, 55 : 2028 - 2030
  • [10] Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli
    Lohkamp, B
    Coggins, JR
    Lapthorn, AJ
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 : 1488 - 1491